ID   VLDC_STRHL              Reviewed;         351 AA.
AC   Q15JG5;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=C(7)-cyclitol 7-kinase {ECO:0000250|UniProtKB:Q3T6E2};
DE            EC=2.7.1.214 {ECO:0000250|UniProtKB:Q3T6E2};
GN   Name=vldC {ECO:0000312|EMBL:ABC67265.1};
GN   ORFNames=SHL15_8010 {ECO:0000312|EMBL:ALO98987.1};
OS   Streptomyces hygroscopicus subsp. limoneus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=264445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 21432 / NBRC 12704 / KCTC 1717 / KCCM 11405;
RX   PubMed=16725283; DOI=10.1016/j.gene.2005.12.035;
RA   Singh D., Seo M.J., Kwon H.J., Rajkarnikar A., Kim K.R., Kim S.O.,
RA   Suh J.W.;
RT   "Genetic localization and heterologous expression of validamycin
RT   biosynthetic gene cluster isolated from Streptomyces hygroscopicus var.
RT   limoneus KCCM 11405 (IFO 12704).";
RL   Gene 376:13-23(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21432 / NBRC 12704 / KCTC 1717 / KCCM 11405
RC   {ECO:0000312|Proteomes:UP000057753}, and
RC   KCTC 1717 {ECO:0000312|EMBL:ALO98987.1};
RA   Kim K.M.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of the antifungal agent
CC       validamycin A (PubMed:16725283). Catalyzes the phosphorylation of
CC       valienone and validone to their 7-phosphate derivatives (By
CC       similarity). {ECO:0000250|UniProtKB:Q3T6E2,
CC       ECO:0000269|PubMed:16725283}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + valienone = ADP + H(+) + valienone 7-phosphate;
CC         Xref=Rhea:RHEA:49420, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:111521, ChEBI:CHEBI:111522, ChEBI:CHEBI:456216;
CC         EC=2.7.1.214; Evidence={ECO:0000250|UniProtKB:Q3T6E2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + validone = ADP + H(+) + validone 7-phosphate;
CC         Xref=Rhea:RHEA:49424, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:111523, ChEBI:CHEBI:111542, ChEBI:CHEBI:456216;
CC         EC=2.7.1.214; Evidence={ECO:0000250|UniProtKB:Q3T6E2};
CC   -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR   EMBL; DQ223652; ABC67265.1; -; Genomic_DNA.
DR   EMBL; CP013220; ALO98987.1; -; Genomic_DNA.
DR   RefSeq; WP_058084466.1; NZ_CP013220.1.
DR   AlphaFoldDB; Q15JG5; -.
DR   SMR; Q15JG5; -.
DR   EnsemblBacteria; ALO98987; ALO98987; SHL15_8010.
DR   PATRIC; fig|264445.3.peg.8523; -.
DR   BRENDA; 2.7.1.214; 14504.
DR   Proteomes; UP000057753; Chromosome II.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000600; ROK.
DR   PANTHER; PTHR18964; PTHR18964; 1.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Kinase; Transferase.
FT   CHAIN           1..351
FT                   /note="C(7)-cyclitol 7-kinase"
FT                   /id="PRO_0000443534"
SQ   SEQUENCE   351 AA;  35935 MW;  20B449E04DE1D848 CRC64;
     MTALTPAPCD LVVADLGGTT LRVGRITAGT SEVHDVKRVP TNGLGRYGAL APQELQDRVM
     EQLTREIAAH LNRPGQAPAQ AVAVSFAGPM TADGVVLAGP TLWGGPAAPL PVADVLTQQL
     GLPVVAANDV TAAAWRYAAA EPEPFCLTTV SSGIGNKVFR HGEIVIDQLG YGGEIGHWLV
     DHAEDAAPCE CGGRGHLGAI ASGRGALFAV RAAAAADASA FARSALAGPS GGVPEAITNE
     AFAAAARAGD TFARESLRRS LRPLASAVSL LFTAIGVRRY LFVGGFALAL GDTFLTLLGD
     ELVRVGCFGL DEYATRAMLA LGEDDDDHCL IGIGQLAAAR LGAPRAVEVT A